PRPH2_CHICK
ID PRPH2_CHICK Reviewed; 354 AA.
AC O42281;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Peripherin-2;
DE AltName: Full=CRDS1;
DE AltName: Full=Photoreceptor outer segment membrane glycoprotein 1;
DE AltName: Full=Retinal degeneration slow protein;
GN Name=PRPH2; Synonyms=RDS;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=9478005;
RA Weng J., Belecky-Adams T., Adler R., Travis G.H.;
RT "Identification of two rds/peripherin homologs in the chick retina.";
RL Invest. Ophthalmol. Vis. Sci. 39:440-443(1998).
CC -!- FUNCTION: May be involved in the morphogenesis of retina outer segment
CC disks and the development and maintenance of the retina ultrastructure.
CC {ECO:0000250|UniProtKB:P15499}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P17810}; Multi-
CC pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the PRPH2/ROM1 family. {ECO:0000305}.
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DR EMBL; AF031238; AAC06274.1; -; mRNA.
DR RefSeq; NP_990369.1; NM_205038.1.
DR AlphaFoldDB; O42281; -.
DR STRING; 9031.ENSGALP00000016098; -.
DR PaxDb; O42281; -.
DR Ensembl; ENSGALT00000016117; ENSGALP00000016098; ENSGALG00000009909.
DR GeneID; 395899; -.
DR KEGG; gga:395899; -.
DR CTD; 5961; -.
DR VEuPathDB; HostDB:geneid_395899; -.
DR eggNOG; KOG3882; Eukaryota.
DR GeneTree; ENSGT00940000157303; -.
DR HOGENOM; CLU_068903_0_0_1; -.
DR InParanoid; O42281; -.
DR OMA; TDIMAKM; -.
DR OrthoDB; 1470436at2759; -.
DR PhylomeDB; O42281; -.
DR TreeFam; TF331684; -.
DR PRO; PR:O42281; -.
DR Proteomes; UP000000539; Chromosome 3.
DR Bgee; ENSGALG00000009909; Expressed in spermatid and 1 other tissue.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; IEA:Ensembl.
DR GO; GO:0035845; P:photoreceptor cell outer segment organization; IEA:Ensembl.
DR GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
DR GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
DR GO; GO:0060041; P:retina development in camera-type eye; ISS:UniProtKB.
DR CDD; cd03162; peripherin_like_LEL; 1.
DR Gene3D; 1.10.1450.10; -; 1.
DR InterPro; IPR000830; Peripherin/rom-1.
DR InterPro; IPR018498; Peripherin/rom-1_CS.
DR InterPro; IPR042026; Peripherin_LEL.
DR InterPro; IPR018499; Tetraspanin/Peripherin.
DR InterPro; IPR008952; Tetraspanin_EC2_sf.
DR PANTHER; PTHR19282; PTHR19282; 1.
DR Pfam; PF00335; Tetraspanin; 1.
DR PRINTS; PR00218; PERIPHERNRDS.
DR SUPFAM; SSF48652; SSF48652; 1.
DR PROSITE; PS00930; RDS_ROM1; 1.
PE 2: Evidence at transcript level;
KW Cell adhesion; Disulfide bond; Glycoprotein; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..354
FT /note="Peripherin-2"
FT /id="PRO_0000168108"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..61
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..264
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..354
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 335..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 354 AA; 40208 MW; 5100F0DF6A9C96C1 CRC64;
MALLKVKFNQ KKRVKLAQGL WLMNWFSVFA GIIVFSMGLF LKIELRKRSE VMDNSESHFV
PNSLILMGIL SCAFNGFAGK ICYDSLDPAK FAKWKPLLKP YLALCFFFNI LLFFVALICF
LMRGSLESTL AQGLKNSMKF YRDTDTPGRC FMKKTIDMLQ IEFKCCGNNG FKDWFEIQWI
SNRYLDFSSK EVKDRIKSNV DGRYLVDGVP FSCCNPSSPR PCIQYQVTNN SAHYSYDYQT
EELNLWGRGC REALLHYYSS MMSSMGAVVL LVWLFEMSVM VGLRLLHTSL ESIANPEDPE
CESEGWILEN SLKDTLKSAL ESLKKIGKFN QVEAGAEGAE GEEAGKTPAI TTVS
